View source for 9ka5


==Crystal structure of beta-ketoacyl-ACP synthase FabH C112Q from E. coli==
<StructureSection load='9ka5' size='340' side='right'caption='[[9ka5]], [[Resolution|resolution]] 1.42&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9ka5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9KA5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9KA5 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.42&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9ka5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9ka5 OCA], [https://pdbe.org/9ka5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9ka5 RCSB], [https://www.ebi.ac.uk/pdbsum/9ka5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9ka5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FABH_ECOLI FABH_ECOLI] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for acetyl-CoA. Its substrate specificity determines the biosynthesis of straight-chain of fatty acids instead of branched-chain.[HAMAP-Rule:MF_01815]
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Cai C]]
[[Category: Zhang L]]